[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00014932; PubMed=8507827 [NCBI, ExPASy, EBI, Israel, Japan] Junghans H., Dalkin K., Dixon R.A.; "Stress responses in alfalfa (Medicago sativa L.). 15. Characterization and expression patterns of members of a subset of the chalcone synthase multigene family."; Plant Mol. Biol. 22:239-253(1993).
[2]	X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS). DOI=10.1021/bi991489f; PubMed=10653632 [NCBI, ExPASy, EBI, Israel, Japan] Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., Noel J.P.; "Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase."; Biochemistry 39:890-902(2000).

Comments

FUNCTION: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
CATALYTIC ACTIVITY: 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO₂.
PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis .
SIMILARITY: Belongs to the chalcone/stilbene synthases family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L02902; AAA02824.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S35164; S35164.

3D structure databases

PDB

1BI5; X-ray; 1.56 A; A=1-389.	[ExPASy / RCSB / EBI]
1BQ6; X-ray; 1.56 A; A=2-389.	[ExPASy / RCSB / EBI]
1CGK; X-ray; 1.84 A; A=1-389.	[ExPASy / RCSB / EBI]
1CGZ; X-ray; 1.70 A; A=1-389.	[ExPASy / RCSB / EBI]
1CHW; X-ray; 1.90 A; A/B=1-389.	[ExPASy / RCSB / EBI]
1CML; X-ray; 1.69 A; A=1-389.	[ExPASy / RCSB / EBI]
1D6F; X-ray; 1.69 A; A=1-389.	[ExPASy / RCSB / EBI]
1D6H; X-ray; 2.15 A; A=3-389.	[ExPASy / RCSB / EBI]
1D6I; X-ray; 2.00 A; A/B=2-389.	[ExPASy / RCSB / EBI]
1I86; X-ray; 1.50 A; A=1-389.	[ExPASy / RCSB / EBI]
1I88; X-ray; 1.45 A; A/B=1-389.	[ExPASy / RCSB / EBI]
1I89; X-ray; 1.86 A; A/B=1-389.	[ExPASy / RCSB / EBI]
1I8B; X-ray; 1.95 A; A/B=1-389.	[ExPASy / RCSB / EBI]
1JWX; X-ray; 1.63 A; A=1-389.	[ExPASy / RCSB / EBI]
1U0V; X-ray; 1.90 A; A/B=1-389.	[ExPASy / RCSB / EBI]
1U0W; X-ray; 2.00 A; A/B/C/D=1-389.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BI5; -.
1BQ6; -.
1CGK; -.
1CGZ; -.
1CHW; -.
1CML; -.
1D6F; -.
1D6H; -.
1D6I; -.
1I86; -.
1I88; -.
1I89; -.
1I8B; -.
1JWX; -.
1U0V; -.
1U0W; -.

ModBase

P30074.

Ontologies

GO:0008415;	Molecular function: acyltransferase activity (inferred from electronic annotation from InterPro).
GO:0016210;	Molecular function: naringenin-chalcone synthase activity (inferred from electronic annotation from EC).
GO:0009813;	Biological process: flavonoid biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR012328; Chal_sti_synt_C.
IPR001099; Chal_sti_synt_N.
IPR011141; Polyketide_synthase_type-III.
IPR016038; Thiolase-like_subgr.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.47.10; Thiolase-like_subgr; 2.

Pfam

PF02797; Chal_sti_synt_C; 1.
PF00195; Chal_sti_synt_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000451; PKS_III; 1.

ProDom

PD000453; N-C_synthase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00441; CHALCONE_SYNTH; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acyltransferase; Flavonoid biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 389`	`389`	`Chalcone synthase 2.`	`PRO_0000216007`
`ACT_SITE`	`164 164`
`HELIX`	`4 11`	`8`
`STRAND`	`18 25`	`8`
`STRAND`	`30 32`	`3`
`HELIX`	`33 35`	`3`
`HELIX`	`36 43`	`8`
`HELIX`	`50 62`	`13`
`STRAND`	`67 69`	`3`
`HELIX`	`74 79`	`6`
`HELIX`	`81 84`	`4`
`STRAND`	`85 87`	`3`
`HELIX`	`91 117`	`27`
`HELIX`	`121 123`	`3`
`STRAND`	`126 133`	`8`
`HELIX`	`140 148`	`9`
`STRAND`	`155 161`	`7`
`HELIX`	`166 179`	`14`
`STRAND`	`185 192`	`8`
`HELIX`	`194 196`	`3`
`HELIX`	`206 214`	`9`
`STRAND`	`218 227`	`10`
`TURN`	`230 232`	`3`
`STRAND`	`237 246`	`10`
`STRAND`	`253 259`	`7`
`STRAND`	`262 267`	`6`
`HELIX`	`271 287`	`17`
`HELIX`	`288 290`	`3`
`STRAND`	`297 302`	`6`
`HELIX`	`307 317`	`11`
`HELIX`	`321 324`	`4`
`HELIX`	`325 334`	`10`
`HELIX`	`338 340`	`3`
`HELIX`	`341 355`	`15`
`TURN`	`361 364`	`4`
`STRAND`	`366 374`	`9`
`TURN`	`375 377`	`3`
`STRAND`	`378 386`	`9`

Sequence information

Length: 389 AA [This is the length of the unprocessed precursor]

Molecular weight: 42706 Da [This is the MW of the unprocessed precursor]

CRC64: E03422EE332A5408 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSVSEIRKA QRAEGPATIL AIGTANPANC VEQSTYPDFY FKITNSEHKT ELKEKFQRMC 

        70         80         90        100        110        120 
DKSMIKRRYM YLTEEILKEN PNVCEYMAPS LDARQDMVVV EVPRLGKEAA VKAIKEWGQP 

       130        140        150        160        170        180 
KSKITHLIVC TTSGVDMPGA DYQLTKLLGL RPYVKRYMMY QQGCFAGGTV LRLAKDLAEN 

       190        200        210        220        230        240 
NKGARVLVVC SEVTAVTFRG PSDTHLDSLV GQALFGDGAA ALIVGSDPVP EIEKPIFEMV 

       250        260        270        280        290        300 
WTAQTIAPDS EGAIDGHLRE AGLTFHLLKD VPGIVSKNIT KALVEAFEPL GISDYNSIFW 

       310        320        330        340        350        360 
IAHPGGPAIL DQVEQKLALK PEKMNATREV LSEYGNMSSA CVLFILDEMR KKSTQNGLKT 

       370        380 
TGEGLEWGVL FGFGPGLTIE TVVLRSVAI

P30074 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools